P46821 (MAP1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Microtubule-associated protein 1B
Short name=MAP-1B

Cleaved into the following 2 chains:

1. MAP1B heavy chain
2. MAP1 light chain LC1

Gene names

Name:

MAP1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Facilitates tyrosination of alpha-tubulin in neuronal microtubules By similarity. Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B Binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. Ref.13
Subunit structure	3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts with the tubulin tyrosine TTL By similarity. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1. Ref.7 Ref.8 Ref.13
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm. Cell junction › synapse By similarity. Cell projection › dendritic spine By similarity. Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers By similarity. Ref.13
Domain	Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules.
Post-translational modification	LC1 is generated from MAP1B by proteolytic processing. S-nitrosylation at Cys-2464 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction By similarity.
Sequence similarities	Belongs to the MAP1 family.

Ontologies

Keywords
Cellular component	Cell junction Cell projection Cytoplasm Cytoskeleton Microtubule Synapse
Coding sequence diversity	Polymorphism
Domain	Repeat
PTM	Acetylation Phosphoprotein S-nitrosylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	axonogenesis Inferred from electronic annotation. Source: Compara cellular process Inferred from direct assay PubMed 19567321. Source: DFLAT dendrite development Inferred from electronic annotation. Source: Compara establishment of monopolar cell polarity Inferred from electronic annotation. Source: Compara microtubule bundle formation Inferred from electronic annotation. Source: Compara mitochondrion transport along microtubule Inferred from electronic annotation. Source: Compara negative regulation of intracellular transport Inferred from electronic annotation. Source: Compara positive regulation of axon extension Inferred from electronic annotation. Source: Compara
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Inferred from electronic annotation. Source: Compara dendritic spine Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Traceable author statement PubMed 1881920. Source: ProtInc plasma membrane Inferred from direct assay PubMed 19567321. Source: DFLAT synapse Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	structural molecule activity Non-traceable author statement PubMed 1881920. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GAN	Q9H2C0	3	EBI-764611,EBI-764342

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.5
	Chain	2 – 2468	2467	Microtubule-associated protein 1B		PRO_0000018604
	Chain	2 – 2206	2205	MAP1B heavy chain		PRO_0000418379
	Chain	2207 – 2468	262	MAP1 light chain LC1		PRO_0000018605
Regions
	Repeat	1878 – 1894	17	MAP1B 1
	Repeat	1895 – 1911	17	MAP1B 2
	Repeat	1912 – 1928	17	MAP1B 3
	Repeat	1929 – 1945	17	MAP1B 4
	Repeat	1946 – 1962	17	MAP1B 5
	Repeat	1963 – 1979	17	MAP1B 6
	Repeat	1997 – 2013	17	MAP1B 7
	Repeat	2014 – 2030	17	MAP1B 8
	Repeat	2031 – 2047	17	MAP1B 9
	Repeat	2048 – 2064	17	MAP1B 10
	Compositional bias	589 – 790	202	Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.5 Ref.20
	Modified residue	336	1	Phosphoserine Ref.11
	Modified residue	527	1	Phosphothreonine By similarity
	Modified residue	541	1	Phosphoserine By similarity
	Modified residue	544	1	Phosphoserine By similarity
	Modified residue	561	1	Phosphoserine By similarity
	Modified residue	614	1	Phosphoserine By similarity
	Modified residue	828	1	Phosphoserine Ref.20
	Modified residue	831	1	Phosphoserine Ref.18 Ref.20
	Modified residue	832	1	Phosphoserine Ref.18 Ref.20
	Modified residue	937	1	Phosphoserine Ref.20
	Modified residue	992	1	Phosphoserine Ref.9 Ref.20
	Modified residue	995	1	Phosphoserine Ref.9 Ref.20
	Modified residue	1016	1	Phosphoserine Ref.9 Ref.16 Ref.20
	Modified residue	1144	1	Phosphoserine Ref.20
	Modified residue	1154	1	Phosphoserine Ref.20
	Modified residue	1156	1	Phosphoserine Ref.20
	Modified residue	1208	1	Phosphoserine Ref.20
	Modified residue	1252	1	Phosphoserine Ref.20
	Modified residue	1256	1	Phosphoserine Ref.20
	Modified residue	1260	1	Phosphoserine Ref.20
	Modified residue	1265	1	Phosphoserine Ref.9 Ref.20
	Modified residue	1276	1	Phosphoserine Ref.9
	Modified residue	1280	1	Phosphoserine Ref.9
	Modified residue	1282	1	Phosphothreonine Ref.9 Ref.20
	Modified residue	1312	1	Phosphoserine By similarity
	Modified residue	1322	1	Phosphoserine By similarity
	Modified residue	1324	1	Phosphoserine By similarity
	Modified residue	1336	1	Phosphotyrosine By similarity
	Modified residue	1337	1	Phosphotyrosine By similarity
	Modified residue	1339	1	Phosphoserine By similarity
	Modified residue	1376	1	Phosphoserine By similarity
	Modified residue	1378	1	Phosphoserine Ref.20
	Modified residue	1387	1	Phosphoserine Ref.20
	Modified residue	1389	1	Phosphoserine Ref.20
	Modified residue	1396	1	Phosphoserine Ref.9 Ref.18
	Modified residue	1400	1	Phosphoserine Ref.9 Ref.18 Ref.20
	Modified residue	1408	1	Phosphoserine By similarity
	Modified residue	1427	1	Phosphoserine Ref.9 Ref.14 Ref.20
	Modified residue	1438	1	Phosphoserine Ref.9 Ref.20
	Modified residue	1443	1	Phosphoserine Ref.9 Ref.20
	Modified residue	1501	1	Phosphoserine Ref.18 Ref.20
	Modified residue	1618	1	Phosphoserine Ref.9
	Modified residue	1620	1	Phosphoserine Ref.9
	Modified residue	1625	1	Phosphoserine Ref.9
	Modified residue	1653	1	Phosphoserine Ref.20
	Modified residue	1772	1	Phosphoserine By similarity
	Modified residue	1779	1	Phosphoserine Ref.9 Ref.17 Ref.20
	Modified residue	1782	1	Phosphoserine Ref.9 Ref.20
	Modified residue	1785	1	Phosphoserine Ref.20
	Modified residue	1788	1	Phosphothreonine Ref.9 Ref.20
	Modified residue	1793	1	Phosphoserine By similarity
	Modified residue	1796	1	Phosphotyrosine By similarity
	Modified residue	1797	1	Phosphoserine Ref.20
	Modified residue	1817	1	Phosphoserine By similarity
	Modified residue	1819	1	Phosphoserine By similarity
	Modified residue	1881	1	Phosphoserine By similarity
	Modified residue	1915	1	Phosphoserine Ref.20
	Modified residue	1917	1	Phosphoserine Ref.20
	Modified residue	1932	1	Phosphothreonine By similarity
	Modified residue	1949	1	Phosphothreonine By similarity
	Modified residue	1965	1	Phosphoserine Ref.20
	Modified residue	2072	1	Phosphoserine By similarity
	Modified residue	2098	1	Phosphoserine By similarity
	Modified residue	2271	1	Phosphoserine Ref.20
	Modified residue	2289	1	Phosphoserine Ref.20
	Modified residue	2464	1	S-nitrosocysteine By similarity
Natural variations
	Natural variant	326	1	R → Q in a colorectal cancer sample; somatic mutation. Ref.21		VAR_036016
	Natural variant	574	1	V → M in a colorectal cancer sample; somatic mutation. Ref.21		VAR_036017
	Natural variant	594	1	I → V. Ref.1 Ref.2 Ref.4 Corresponds to variant rs1866374 [ dbSNP | Ensembl ].		VAR_024530
	Natural variant	869	1	E → G. Corresponds to variant rs16876070 [ dbSNP | Ensembl ].		VAR_030347
	Natural variant	1296	1	P → L. Corresponds to variant rs34093016 [ dbSNP | Ensembl ].		VAR_034105
	Natural variant	1917	1	S → R. Corresponds to variant rs13153166 [ dbSNP | Ensembl ].		VAR_056123

Sequences

	Sequence		Length	Mass (Da)
	P46821 [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 3FFDCB2E20049A8A	FASTA	2,468	270,634
	10 20 30 40 50 60 MATVVVEATE PEPSGSIANP AASTSPSLSH RFLDSKFYLL VVVGEIVTEE HLRRAIGNIE 70 80 90 100 110 120 LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV 130 140 150 160 170 180 STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP 190 200 210 220 230 240 ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP 250 260 270 280 290 300 SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 310 320 330 340 350 360 LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEEQSQGST TNSDWMKNLI SPDLGVVFLN 370 380 390 400 410 420 VPENLKNPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIDPVI LFQKMGVGKL 430 440 450 460 470 480 EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE FILPNGQEVD LPISYLTSVS SLIVWHPANP 490 500 510 520 530 540 AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPVV KQTKLKQRAD 550 560 570 580 590 600 SRESLKPAAK PLPSKSVRKE SKEETPEVTK VNHVEKPPKV ESKEKVMVKK DKPIKTETKP 610 620 630 640 650 660 SVTEKEVPSK EEPSPVKAEV AEKQATDVKP KAAKEKTVKK ETKVKPEDKK EEKEKPKKEV 670 680 690 700 710 720 AKKEDKTPIK KEEKPKKEEV KKEVKKEIKK EEKKEPKKEV KKETPPKEVK KEVKKEEKKE 730 740 750 760 770 780 VKKEEKEPKK EIKKLPKDAK KSSTPLSEAK KPAALKPKVP KKEESVKKDS VAAGKPKEKG 790 800 810 820 830 840 KIKVIKKEGK AAEAVAAAVG TGATTAAVMA AAGIAAIGPA KELEAERSLM SSPEDLTKDF 850 860 870 880 890 900 EELKAEEVDV TKDIKPQLEL IEDEEKLKET EPVEAYVIQK EREVTKGPAE SPDEGITTTE 910 920 930 940 950 960 GEGECEQTPE ELEPVEKQGV DDIEKFEDEG AGFEESSETG DYEEKAETEE AEEPEEDGEE 970 980 990 1000 1010 1020 HVCVSASKHS PTEDEESAKA EADAYIREKR ESVASGDDRA EEDMDEAIEK GEAEQSEEEA 1030 1040 1050 1060 1070 1080 DEEDKAEDAR EEEYEPEKME AEDYVMAVVD KAAEAGGAEE QYGFLTTPTK QLGAQSPGRE 1090 1100 1110 1120 1130 1140 PASSIHDETL PGGSESEATA SDEENREDQP EEFTATSGYT QSTIEISSEP TPMDEMSTPR 1150 1160 1170 1180 1190 1200 DVMSDETNNE ETESPSQEFV NITKYESSLY SQEYSKPADV TPLNGFSEGS KTDATDGKDY 1210 1220 1230 1240 1250 1260 NASASTISPP SSMEEDKFSR SALRDAYCSE VKASTTLDIK DSISAVSSEK VSPSKSPSLS 1270 1280 1290 1300 1310 1320 PSPPSPLEKT PLGERSVNFS LTPNEIKVSA EAEVAPVSPE VTQEVVEEHC ASPEDKTLEV 1330 1340 1350 1360 1370 1380 VSPSQSVTGS AGHTPYYQSP TDEKSSHLPT EVIEKPPAVP VSFEFSDAKD ENERASVSPM 1390 1400 1410 1420 1430 1440 DEPVPDSESP IEKVLSPLRS PPLIGSESAY ESFLSADDKA SGRGAESPFE EKSGKQGSPD 1450 1460 1470 1480 1490 1500 QVSPVSEMTS TSLYQDKQEG KSTDFAPIKE DFGQEKKTDD VEAMSSQPAL ALDERKLGDV 1510 1520 1530 1540 1550 1560 SPTQIDVSQF GSFKEDTKMS ISEGTVSDKS ATPVDEGVAE DTYSHMEGVA SVSTASVATS 1570 1580 1590 1600 1610 1620 SFPEPTTDDV SPSLHAEVGS PHSTEVDDSL SVSVVQTPTT FQETEMSPSK EECPRPMSIS 1630 1640 1650 1660 1670 1680 PPDFSPKTAK SRTPVQDHRS EQSSMSIEFG QESPEQSLAM DFSRQSPDHP TVGAGVLHIT 1690 1700 1710 1720 1730 1740 ENGPTEVDYS PSDMQDSSLS HKIPPMEEPS YTQDNDLSEL ISVSQVEASP STSSAHTPSQ 1750 1760 1770 1780 1790 1800 IASPLQEDTL SDVAPPRDMS LYASLTSEKV QSLEGEKLSP KSDISPLTPR ESSPLYSPTF 1810 1820 1830 1840 1850 1860 SDSTSAVKEK TATCHSSSSP PIDAASAEPY GFRASVLFDT MQHHLALNRD LSTPGLEKDS 1870 1880 1890 1900 1910 1920 GGKTPGDFSY AYQKPEETTR SPDEEDYDYE SYEKTTRTSD VGGYYYEKIE RTTKSPSDSG 1930 1940 1950 1960 1970 1980 YSYETIGKTT KTPEDGDYSY EIIEKTTRTP EEGGYSYDIS EKTTSPPEVS GYSYEKTERS 1990 2000 2010 2020 2030 2040 RRLLDDISNG YDDSEDGGHT LGDPSYSYET TEKITSFPES EGYSYETSTK TTRTPDTSTY 2050 2060 2070 2080 2090 2100 CYETAEKITR TPQASTYSYE TSDLCYTAEK KSPSEARQDV DLCLVSSCEY KHPKTELSPS 2110 2120 2130 2140 2150 2160 FINPNPLEWF ASEEPTEESE KPLTQSGGAP PPPGGKQQGR QCDETPPTSV SESAPSQTDS 2170 2180 2190 2200 2210 2220 DVPPETEECP SITADANIDS EDESETIPTD KTVTYKHMDP PPAPVQDRSP SPRHPDVSMV 2230 2240 2250 2260 2270 2280 DPEALAIEQN LGKALKKDLK EKTKTKKPGT KTKSSSPVKK SDGKSKPLAA SPKPAGLKES 2290 2300 2310 2320 2330 2340 SDKVSRVASP KKKESVEKAA KPTTTPEVKA ARGEEKDKET KNAANASASK SAKTATAGPG 2350 2360 2370 2380 2390 2400 TTKTTKSSAV PPGLPVYLDL CYIPNHSNSK NVDVEFFKRV RSSYYVVSGN DPAAEEPSRA 2410 2420 2430 2440 2450 2460 VLDALLEGKA QWGSNMQVTL IPTHDSEVMR EWYQETHEKQ QDLNIMVLAS SSTVVMQDES FPACKIEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human microtubule-associated protein 1B and the identification of a related gene on chromosome 15." Lien L.L., Feener C., Fischbach N., Kunkel L.M. Genomics 22:273-280(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594. Tissue: Fetal brain.
[2]	"Hmob3 brain-specific sequence is a part of phylogenetically conserved human MAP1B gene 3'-untranslated region." Dergunova L.V., Raevskaya N.M., Vladychenskaya I.P., Limborska S.A. Biomol. Eng. 20:91-96(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-594.
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT VAL-594.
[5]	Bienvenut W.V., Pchelintsev N., Adams P.D. Submitted (OCT-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-31; 55-64; 90-98; 391-429; 520-531; 1052-1070; 1233-1250; 1276-1287; 1462-1476; 1834-1958 AND 1898-1908, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Lung fibroblast.
[6]	Lubec G., Afjehi-Sadat L., Vishwanath V., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2347-2370 AND 2382-2409, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[7]	"Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin." Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y. J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAN.
[8]	"Gigaxonin-controlled degradation of MAP1B light chain is critical to neuronal survival." Allen E., Ding J., Wang W., Pramanik S., Chou J., Yau V., Yang Y. Nature 438:224-228(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH GAN.
[9]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-992; SER-995; SER-1016; SER-1265; SER-1276; SER-1280; THR-1282; SER-1396; SER-1400; SER-1427; SER-1438; SER-1443; SER-1618; SER-1620; SER-1625; SER-1779; SER-1782 AND THR-1788, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line." Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S. Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Prostate cancer.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-336, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH reveals heavy- and light-chain subunits generated by proteolytic processing at a conserved cleavage site." Zou B., Yan H., Kawasaki F., Ordway R.W. Biochem. J. 414:63-71(2008) [PubMed] [Europe PMC] [Abstract] Cited for: CLEAVAGE SITE.
[13]	"DAPK-1 binding to a linear peptide motif in MAP1B stimulates autophagy and membrane blebbing." Harrison B., Kraus M., Burch L., Stevens C., Craig A., Gordon-Weeks P., Hupp T.R. J. Biol. Chem. 283:9999-10014(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH DAPK1.
[14]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1427, MASS SPECTROMETRY. Tissue: Platelet.
[15]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography." Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J. Proteomics 8:1346-1361(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1016, MASS SPECTROMETRY. Tissue: Liver.
[17]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1779, MASS SPECTROMETRY.
[18]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-831; SER-832; SER-1396; SER-1400 AND SER-1501, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-828; SER-831; SER-832; SER-937; SER-992; SER-995; SER-1016; SER-1144; SER-1154; SER-1156; SER-1208; SER-1252; SER-1256; SER-1260; SER-1265; THR-1282; SER-1378; SER-1387; SER-1389; SER-1400; SER-1427; SER-1438; SER-1443; SER-1501; SER-1653; SER-1779; SER-1782; SER-1785; THR-1788; SER-1797; SER-1915; SER-1917; SER-1965; SER-2271 AND SER-2289, MASS SPECTROMETRY.
[21]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-326 AND MET-574.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L06237 mRNA. Translation: AAA18904.1. BN001084 mRNA. Translation: CAM06633.1. AC012609 Genomic DNA. No translation available. AC093218 Genomic DNA. No translation available. CH471084 Genomic DNA. Translation: EAW95697.1.
IPI	IPI00008868.
RefSeq	NP_005900.2. NM_005909.3.
UniGene	Hs.335079.
3D structure databases
ProteinModelPortal	P46821.
ModBase	Search...
Protein-protein interaction databases
IntAct	P46821. 23 interactions.
MINT	MINT-243072.
STRING	9606.ENSP00000296755.
PTM databases
PhosphoSite	P46821.
Polymorphism databases
DMDM	1170875.
Proteomic databases
PaxDb	P46821.
PRIDE	P46821.
Protocols and materials databases
DNASU	4131.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000296755; ENSP00000296755; ENSG00000131711.
GeneID	4131.
KEGG	hsa:4131.
UCSC	uc003kbw.4. human.
Organism-specific databases
CTD	4131.
GeneCards	GC05P071438.
HGNC	HGNC:6836. MAP1B.
HPA	CAB009792. HPA022275.
MIM	157129. gene.
neXtProt	NX_P46821.
PharmGKB	PA30581.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOGENOM	HOG000063256.
HOVERGEN	HBG052409.
InParanoid	P46821.
KO	K10429.
OMA	RTPVQDH.
OrthoDB	EOG44XJFW.
PhylomeDB	P46821.
Enzyme and pathway databases
Pathway_Interaction_DB	lis1pathway. Lissencephaly gene (LIS1) in neuronal migration and development. reelinpathway. Reelin signaling pathway.
Gene expression databases
ArrayExpress	P46821.
Bgee	P46821.
CleanEx	HS_MAP1B.
Genevestigator	P46821.
GermOnline	ENSG00000131711. Homo sapiens.
Family and domain databases
InterPro	IPR026074. MAP1. IPR027321. MAP1B. IPR000102. MAP1B_neuraxin. [Graphical view]
PANTHER	PTHR13843. PTHR13843. 1 hit. PTHR13843:SF5. PTHR13843:SF5. 1 hit.
Pfam	PF00414. MAP1B_neuraxin. 5 hits. [Graphical view]
PROSITE	PS00230. MAP1B_NEURAXIN. 6 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MAP1B. human.
GenomeRNAi	4131.
NextBio	16218.
SOURCE	Search...

Entry information

Entry name

MAP1B_HUMAN

Accession

Primary (citable) accession number: P46821
Secondary accession number(s): A2BDK5

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 11, 2011
Last modified:	May 1, 2013
This is version 120 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.